Phytepsin

Phytepsin (EC 3.4.23.40) is an enzyme.[1][2][3][4] This enzyme catalyses the following chemical reaction

Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-Asp- and -Asp-Asp- bonds in 2S albumin from plant seeds
Phytepsin
Identifiers
EC number3.4.23.40
CAS number219715-98-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Phytepsin
Identifiers
Symbolphytepsin
InterProIPR033869
CDDcd06098

This enzyme is present in barley grain and other plants. It is an aspartic protease with a plant-specific insert.

References
  1. Runeberg-Roos P, Törmäkangas K, Ostman A (December 1991). "Primary structure of a barley-grain aspartic proteinase. A plant aspartic proteinase resembling mammalian cathepsin D". European Journal of Biochemistry. 202 (3): 1021–7. doi:10.1111/j.1432-1033.1991.tb16465.x. PMID 1722454.
  2. Kervinen J, Sarkkinen P, Kalkkinen N, Mikola L, Saarma M (March 1993). "Hydrolytic specificity of the barley grain aspartic proteinase". Phytochemistry. 32 (4): 799–803. doi:10.1016/0031-9422(93)85208-9. PMID 7763475.
  3. Asakura T, Watanabe H, Abe K, Arai S (August 1995). "Rice aspartic proteinase, oryzasin, expressed during seed ripening and germination, has a gene organization distinct from those of animal and microbial aspartic proteinases". European Journal of Biochemistry. 232 (1): 77–83. doi:10.1111/j.1432-1033.1995.tb20783.x. PMID 7556174.
  4. Kervinen J, Törmäkangas K, Runeberg-Roos P, Guruprasad K, Blundell T, Teeri TH (1995). "Structure and possible function of aspartic proteinases in barley and other plants". Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology. 362: 241–54. doi:10.1007/978-1-4615-1871-6_28. ISBN 978-1-4613-5761-2. PMID 8540324.
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